Cited by 762Histone Deacetylase Inhibitors ResearchGenomics and Chromatin DynamicsEpigenetics and DNA Methylation

The DOI matches its Crossref record; 60 of the 60 references it cites were found in a registry or an index.

Enzymatic Activity Associated with Class II HDACs Is Dependent on a Multiprotein Complex Containing HDAC3 and SMRT/N-CoR

Open access

Fischle, Wolfgang, Dequiedt, Franck, Hendzel, Michael J, Guenther, Matthew G, Lazar, Mitchell A, Voelter, Wolfgang, Verdin, Eric·2002·Molecular Cell

DOI 10.1016/s1097-2765(01)00429-4

Open this paper in CoChat — free account Open PDF

Abstract

Histone deacetylases (HDACs) play a key role in regulating eukaryotic gene expression. The HDAC domain, homologous to the yeast repressors RPD3 and HDA1, is considered necessary and sufficient for enzymatic activity. Here, we show that the catalytic domain of HDAC4 interacts with HDAC3 via the transcriptional corepressor N-CoR/SMRT. All experimental conditions leading to the suppression of HDAC4 binding to SMRT/N-CoR and to HDAC3 result in the loss of enzymatic activity associated with HDAC4. In vitro reconstitution experiments indicate that HDAC4 and other class II HDACs are inactive in the context of the SMRT/N-CoR-HDAC3 complex and do not contribute to its enzymatic activity. These observations indicate that class II HDACs regulate transcription by bridging the enzymatically active SMRT/N-CoR-HDAC3 complex and select transcription factors independently of any intrinsic HDAC activity.

Integrity signals

Registry

Crossref · 10.1016/s1097-2765(01)00429-4

Cites

60 of 60 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Crystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466
Current protocols in molecular biology
Sargent, T. (1988) · Analytical Biochemistry · doi:10.1016/0003-2697(88)90147-9 · Cited by 7,281
Histone acetylation in chromatin structure and transcription
Grunstein, M. (1997) · Nature · doi:10.1038/38664 · Cited by 2,884
The coregulator exchange in transcriptional functions of nuclear receptors
Glass, C. K., & Rosenfeld, M. G. (2000) · Genes & Development · doi:10.1101/gad.14.2.121 · Cited by 2,233
Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor
Hörlein, A., Näär, A. M., Heinzel, T., Torchia, J., Gloss, B. R., Kurokawa, R., Ryan, A. K., Kamei, Y., Söderström, M., Glass, C. K., et al. (1995) · Nature · doi:10.1038/377397a0 · Cited by 2,072
Twenty-Five Years of the Nucleosome, Fundamental Particle of the Eukaryote Chromosome
Kornberg, R. D., & Lorch, Y. (1999) · Cell · doi:10.1016/s0092-8674(00)81958-3 · Cited by 1,833
A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p
Taunton, J., Hassig, C. A., & Schreiber, S. L. (1996) · Science · doi:10.1126/science.272.5260.408 · Cited by 1,829
Histone acetylation and transcriptional regulatory mechanisms
Struhl, K. (1998) · Genes & Development · doi:10.1101/gad.12.5.599 · Cited by 1,815
Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors
Finnin, M. S., Donigian, J. R., Cohen, A., Richon, V. M., Rifkind, R. A., Marks, P. A., Breslow, R., & Pavletich, N. P. (1999) · Nature · doi:10.1038/43710 · Cited by 1,714
Tumor necrosis factor alpha and interleukin 1 stimulate the human immunodeficiency virus enhancer by activation of the nuclear factor kappa B.
Osborn, L., Kunkel, S. L., & Nabel, G. J. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.7.2336 · Cited by 1,583

Show all 60 references

Sorted by citations

Histone deacetylases (HDACs): characterization of the classical HDAC family
RUIJTER, A. J. M. D., GENNIP, A. H. V., CARON, H. N., KEMP, S., & KUILENBURG, A. B. P. V. (2003) · Biochemical Journal · doi:10.1042/bj20021321 · Cited by 3,114
The many roles of histone deacetylases in development and physiology: implications for disease and therapy
Haberland, M., Montgomery, R. L., & Olson, E. N. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2485 · Cited by 2,600
Anticancer activities of histone deacetylase inhibitors
Bolden, J. E., Peart, M. J., & Johnstone, R. W. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2133 · Cited by 2,919
Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
Minucci, S., & Pelicci, P. G. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1779 · Cited by 2,234
Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders
Falkenberg, K. J., & Johnstone, R. W. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4360 · Cited by 1,564
Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis
Gregoretti, I., Lee, Y.-M., & Goodson, H. V. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.006 · Cited by 1,456
New and emerging HDAC inhibitors for cancer treatment
West, A. C., & Johnstone, R. W. (2014) · Journal of Clinical Investigation · doi:10.1172/jci69738 · Cited by 1,404
The Rpd3/Hda1 family of lysine deacetylases: from bacteria and yeast to mice and men
Yang, X., & Seto, E. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2346 · Cited by 1,277
Determination of the class and isoform selectivity of small-molecule histone deacetylase inhibitors
Khan, N., Jeffers, M., Kumar, S., Hackett, C., Boldog, F., Khramtsov, N., Qian, X., Mills, E., Berghs, S. C., Carey, N., et al. (2008) · Biochemical Journal · doi:10.1042/bj20070779 · Cited by 713
Pathophysiology of cardiac hypertrophy and heart failure: signaling pathways and novel therapeutic targets
Tham, Y. K., Bernardo, B. C., Ooi, J. Y. Y., Weeks, K. L., & McMullen, J. R. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1477-x · Cited by 732
Histone Deacetylases: Unique Players in Shaping the Epigenetic Histone Code
Thiagalingam, S., Cheng, K., Lee, H. J., Mineva, N. D., Thiagalingam, A., & Ponte, J. F. (2003) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2003.tb05964.x · Cited by 700
Class II histone deacetylases: versatile regulators
Verdin, E., Dequiedt, F., & Kasler, H. G. (2003) · Trends in Genetics · doi:10.1016/s0168-9525(03)00073-8 · Cited by 664
Self-citation
Histone Deacetylases 5 and 9 Govern Responsiveness of the Heart to a Subset of Stress Signals and Play Redundant Roles in Heart Development
Chang, S., McKinsey, T. A., Zhang, C. L., Richardson, J. A., Hill, J. A., & Olson, E. N. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.19.8467-8476.2004 · Cited by 612
Histone deacetylase 3 (HDAC3) and other class I HDACs regulate colon cell maturation and p21 expression and are deregulated in human colon cancer
Wilson, A. J., Byun, D.-S., Popova, N., Murray, L. B., L'Italien, K., Sowa, Y., Arango, D., Velcich, A., Augenlicht, L. H., & Mariadason, J. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510023200 · Cited by 575
Class IIa HDAC inhibition reduces breast tumours and metastases through anti-tumour macrophages
Guerriero, J. L., Sotayo, A., Ponichtera, H. E., Castrillon, J. A., Pourzia, A. L., Schad, S., Johnson, S. F., Carrasco, R. D., Lazo, S., Bronson, R. T., et al. (2017) · Nature · doi:10.1038/nature21409 · Cited by 558
Unraveling the hidden catalytic activity of vertebrate class IIa histone deacetylases
Lahm, A., Paolini, C., Pallaoro, M., Nardi, M. C., Jones, P., Neddermann, P., Sambucini, S., Bottomley, M. J., Lo Surdo, P., Carfı́, A., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0706487104 · Cited by 566
Class IIa Histone Deacetylases Are Hormone-Activated Regulators of FOXO and Mammalian Glucose Homeostasis
Mihaylova, M. M., Vasquez, D. S., Ravnskjaer, K., Denechaud, P.-D., Yu, R. T., Alvarez, J. G., Downes, M., Evans, R. M., Montminy, M., & Shaw, R. J. (2011) · Cell · doi:10.1016/j.cell.2011.03.043 · Cited by 533
Deconstructing repression: evolving models of co-repressor action
Perissi, V., Jepsen, K., Glass, C. K., & Rosenfeld, M. G. (2010) · Nature Reviews Genetics · doi:10.1038/nrg2736 · Cited by 532
A short guide to histone deacetylases including recent progress on class II enzymes
Park, S.-Y., & Kim, J. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-0382-4 · Cited by 547
HDAC3 Is a Critical Negative Regulator of Long-Term Memory Formation
McQuown, S. C., Barrett, R. M., Matheos, D. P., Post, R. J., Rogge, G. A., Alenghat, T., Mullican, S. E., Jones, S., Rusche, J. R., Lazar, M. A., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.5052-10.2011 · Cited by 507
Self-citation
Roles of histone deacetylases in epigenetic regulation: emerging paradigms from studies with inhibitors
Delcuve, G. P., Khan, D. H., & Davie, J. R. (2012) · Clinical Epigenetics · doi:10.1186/1868-7083-4-5 · Cited by 505
Histone deacetylases and cancer
Barneda‐Zahonero, B., & Parra, M. (2012) · Molecular Oncology · doi:10.1016/j.molonc.2012.07.003 · Cited by 449
Control of Cardiac Growth by Histone Acetylation/Deacetylation
Backs, J., & Olson, E. N. (2006) · Circulation Research · doi:10.1161/01.res.0000197782.21444.8f · Cited by 440
Class II Histone Deacetylases: from Sequence to Function, Regulation, and Clinical Implication
Yang, X., & Grégoire, S. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.8.2873-2884.2005 · Cited by 428
Epigenetics and cardiovascular disease
Ordovás, J. M., & Smith, C. E. (2010) · Nature Reviews Cardiology · doi:10.1038/nrcardio.2010.104 · Cited by 413
Retinoic acid receptors: From molecular mechanisms to cancer therapy
di Masi, A., Leboffe, L., De Marinis, E., Pagano, F., Cicconi, L., Rochette-Egly, C., Lo-Coco, F., Ascenzi, P., & Nervi, C. (2015) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2014.12.003 · Cited by 403
Chemical mechanisms of histone lysine and arginine modifications
Smith, B. C., & Denu, J. M. (2009) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2008.06.005 · Cited by 390
Epigenetic mechanisms in drug addiction
Renthal, W. R., & Nestler, E. J. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2008.06.004 · Cited by 391
Selective class IIa histone deacetylase inhibition via a nonchelating zinc-binding group
Lobera, M., Madauss, K. P., Pohlhaus, D. T., Wright, Q. G., Trocha, M., Schmidt, D. R., Baloglu, E., Trump, R. P., Head, M. S., Hofmann, G. A., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1223 · Cited by 385
In Vivo Chromatin Remodeling Events Leading to Inflammatory Gene Transcription under Diabetic Conditions
Miao, F., Gonzalo, I. T. G., Lanting, L. L., & Natarajan, R. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311786200 · Cited by 371
Deletion of Histone Deacetylase 3 Reveals Critical Roles in S Phase Progression and DNA Damage Control
Bhaskara, S., Chyla, B., Amann, J. M., Knutson, S. K., Cortez, D., Sun, Z., & Hiebert, S. W. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.02.030 · Cited by 369
Maintenance of cardiac energy metabolism by histone deacetylase 3 in mice
Montgomery, R. L., Potthoff, M. J., Haberland, M., Qi, X., Matsuzaki, S., Humphries, K. M., Richardson, J. A., Bassel‐Duby, R., & Olson, E. N. (2008) · Journal of Clinical Investigation · doi:10.1172/jci35847 · Cited by 365
Regulation of histone deacetylase activities
Sengupta, N., & Seto, E. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20179 · Cited by 357
The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase
Kirsh, O., Seeler, J.-S., Pichler, A., Gast, A., Müller, S. P., Miska, E. A., Marion, M., Harel‐Bellan, A., Kouzarides, T., Melchior, F., et al. (2002) · The EMBO Journal · doi:10.1093/emboj/21.11.2682 · Cited by 328
Injury-Induced HDAC5 Nuclear Export Is Essential for Axon Regeneration
Cho, Y., Sloutsky, R., Naegle, K. M., & Cavalli, V. (2013) · Cell · doi:10.1016/j.cell.2013.10.004 · Cited by 327
The Role of Corepressors in Transcriptional Regulation by Nuclear Hormone Receptors
Privalsky, M. L. (2004) · Annual Review of Physiology · doi:10.1146/annurev.physiol.66.032802.155556 · Cited by 330
Histone modifications affect timing of oligodendrocyte progenitor differentiation in the developing rat brain
Shen, S., Li, J., & Casaccia‐Bonnefil, P. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200412101 · Cited by 336
Structural and Functional Analysis of the Human HDAC4 Catalytic Domain Reveals a Regulatory Structural Zinc-binding Domain
Bottomley, M. J., Surdo, P. L., Giovine, P. D., Cirillo, A., Scarpelli, R., Ferrigno, F., JONES, P. G., Neddermann, P., Francesco, R. D., Steinkühler, C., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803514200 · Cited by 327
Haploinsufficiency of HDAC4 Causes Brachydactyly Mental Retardation Syndrome, with Brachydactyly Type E, Developmental Delays, and Behavioral Problems
Williams, S. R., Aldred, M. A., Der Kaloustian, V. M., Halal, F., Gowans, G., McLeod, D. R., Zondag, S., Toriello, H. V., Magenis, R. E., & Elsea, S. H. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.07.011 · Cited by 302
The Potential of HDAC Inhibitors as Cognitive Enhancers
Gräff, J., & Tsai, L. (2013) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011112-140216 · Cited by 306
Emerging roles of the corepressors NCoR1 and SMRT in homeostasis
Mottis, A., Mouchiroud, L., & Auwerx, J. (2013) · Genes & Development · doi:10.1101/gad.214023.113 · Cited by 297
Exercise-induced histone modifications in human skeletal muscle
McGee, S. L., Fairlie, E., Garnham, A. P., & Hargreaves, M. (2009) · The Journal of Physiology · doi:10.1113/jphysiol.2009.181065 · Cited by 296
The functional interactome landscape of the human histone deacetylase family
Joshi, P., Greco, T. M., Guise, A. J., Luo, Y., Yu, F., Nesvizhskii, A. I., & Cristea, I. M. (2013) · Molecular Systems Biology · doi:10.1038/msb.2013.26 · Cited by 289
Regulation of distinct biological activities of the NF-?B transcription factor complex by acetylation
Chen, L., & Greene, W. C. (2003) · Journal of Molecular Medicine · doi:10.1007/s00109-003-0469-0 · Cited by 275
Liver-specific deletion of histone deacetylase 3 disrupts metabolic transcriptional networks
Knutson, S. K., Chyla, B. J., Amann, J. M., Bhaskara, S., Huppert, S. S., & Hiebert, S. W. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.51 · Cited by 271
Dose-dependent Blockade to Cardiomyocyte Hypertrophy by Histone Deacetylase Inhibitors
Antos, C. L., McKinsey, T. A., Dreitz, M., Hollingsworth, L. M., Zhang, C., Schreiber, K. L., Rindt, H., Gorczynski, R. J., & Olson, E. N. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303113200 · Cited by 269
Substrate binding to histone deacetylases as shown by the crystal structure of the HDAC8–substrate complex
Vannini, A., Volpari, C., Gallinari, P., Jones, P., Mattu, M., Carfí, A., De Francesco, R., Steinkühler, C., & Di Marco, S. (2007) · The EMBO Reports · doi:10.1038/sj.embor.7401047 · Cited by 256
Human HDAC7 Harbors a Class IIa Histone Deacetylase-specific Zinc Binding Motif and Cryptic Deacetylase Activity
Schuetz, A., Min, J., Allali‐Hassani, A., Schapira, M., Shuen, M., Loppnau, P., Mazitschek, R., Kwiatkowski, N. P., Lewis, T. A., Maglathin, R. L., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707362200 · Cited by 266
Histone Deacetylase 6 and Heat Shock Protein 90 Control the Functions of Foxp3 + T-Regulatory Cells
de Zoeten, E. F., Wang, L., Butler, K. V., Beier, U. H., Akimova, T., Sai, H., Bradner, J. E., Mazitschek, R., Kozikowski, A. P., Matthias, P., et al. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05155-11 · Cited by 257
Role for Histone Deacetylase 1 in Human Tumor Cell Proliferation
Senese, S., Zaragoza, K., Minardi, S. P., Muradore, I., Ronzoni, S., Passafaro, A., Bernard, L., Draetta, G. F., Alcalay, M., Seiser, C., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00494-07 · Cited by 253
Deacetylase-Independent Function of HDAC3 in Transcription and Metabolism Requires Nuclear Receptor Corepressor
Sun, Z., Feng, D., Fang, B., Mullican, S. E., You, S.-H., Lim, H., Everett, L. J., Nabel, C. S., Li, Y., Selvakumaran, V., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.10.022 · Cited by 251
Self-citation
A Hormone-Dependent Module Regulating Energy Balance
Wang, B., Moya, N., Niessen, S., Hoover, H. S., Mihaylova, M. M., Shaw, R. J., Yates, J. R., Fischer, W. H., Thomas, J. B., & Montminy, M. (2011) · Cell · doi:10.1016/j.cell.2011.04.013 · Cited by 242
Histone deacetylase 3 coordinates commensal-bacteria-dependent intestinal homeostasis
Alenghat, T., Osborne, L. C., Saenz, S. A., Kobuley, D. E., Ziegler, C. G. K., Mullican, S. E., Choi, I., Grunberg, S., Sinha, R., Wynosky-Dolfi, M. A., et al. (2013) · Nature · doi:10.1038/nature12687 · Cited by 255
Self-citation
Association of Class II Histone Deacetylases with Heterochromatin Protein 1: Potential Role for Histone Methylation in Control of Muscle Differentiation
Zhang, C. L., McKinsey, T. A., & Olson, E. N. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.20.7302-7312.2002 · Cited by 247
Class IIa histone deacetylases: regulating the regulators
Martin, M., Kettmann, R., & Dequiedt, F. (2007) · Oncogene · doi:10.1038/sj.onc.1210613 · Cited by 253
Self-citation
Histone Deacetylase 3 Interacts with Runx2 to Repress the Osteocalcin Promoter and Regulate Osteoblast Differentiation
Schroeder, T. M., Kahler, R. A., Li, X., & Westendorf, J. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403702200 · Cited by 244
Readers, Writers, and Erasers
Gillette, T. G., & Hill, J. A. (2015) · Circulation Research · doi:10.1161/circresaha.116.303630 · Cited by 260
Collaborative spirit of histone deacetylases in regulating chromatin structure and gene expression
Yang, X., & Seto, E. (2003) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(03)00015-7 · Cited by 245
Inhibition of HDAC9 Increases T Regulatory Cell Function and Prevents Colitis in Mice
de Zoeten, E. F., Wang, L., Sai, H., DILLMANN, W. H., & Hancock, W. W. (2009) · Gastroenterology · doi:10.1053/j.gastro.2009.10.037 · Cited by 236
HDAC4: Mechanism of Regulation and Biological Functions
Wang, Z., Qin, G., & Zhao, T. C. (2014) · Epigenomics · doi:10.2217/epi.13.73 · Cited by 239
Therapeutic potential for HDAC inhibitors in the heart
McKinsey, T. A. (2012) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010611-134712 · Cited by 230
Inhibition of Class I Histone Deacetylases Unveils a Mitochondrial Signature and Enhances Oxidative Metabolism in Skeletal Muscle and Adipose Tissue
Galmozzi, A., Mitro, N., Ferrari, A., Gers, E., Gilardi, F., Godio, C., Cermenati, G., Gualerzi, A., Donetti, E., Rotili, D., et al. (2012) · Diabetes · doi:10.2337/db12-0548 · Cited by 242
The nuclear-envelope protein and transcriptional repressor LAP2β interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation
Somech, R., Shaklai, S., Geller, O., Amariglio, N., Simon, A. J., Rechavi, G., & Gal-Yam, E. N. (2005) · Journal of Cell Science · doi:10.1242/jcs.02521 · Cited by 223
The bone morphogenetic protein axis is a positive regulator of skeletal muscle mass
Winbanks, C. E., Chen, J. L., Qian, H., Liu, Y., Bernardo, B. C., Beyer, C., Watt, K. I., Thomson, R. E., Connor, T., Turner, B. J., et al. (2013) · Journal of Cell Biology · doi:10.1083/jcb.201211134 · Cited by 225
HDACs and HDAC inhibitors in colon cancer
Mariadason, J. M. (2008) · Epigenetics · doi:10.4161/epi.3.1.5736 · Cited by 229
Isoform-specific histone deacetylase inhibitors: The next step?
Balasubramanian, S., Verner, E. J., & Buggy, J. J. (2009) · Cancer Letters · doi:10.1016/j.canlet.2009.02.013 · Cited by 228
SMRT Derepression by the IκB Kinase α
Hoberg, J. E., Yeung, F., & Mayo, M. W. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.010 · Cited by 220
Role of Class I and Class II histone deacetylases in carcinoma cells using siRNA
Glaser, K. B., Li, J., Staver, M. J., Wei, R.-Q., Albert, D. H., & Davidsen, S. K. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.09.043 · Cited by 220
Abrogation of TGF-β1-induced fibroblast-myofibroblast differentiation by histone deacetylase inhibition
Guo, W., Shan, B., Klingsberg, R. C., Qin, X., & Lasky, J. A. (2009) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00128.2009 · Cited by 218
Exercise adaptations: molecular mechanisms and potential targets for therapeutic benefit
McGee, S. L., & Hargreaves, M. (2020) · Nature Reviews Endocrinology · doi:10.1038/s41574-020-0377-1 · Cited by 226
Histone deacetylase inhibitors as therapeutics for polyglutamine disorders
Butler, R. K., & Bates, G. P. (2006) · Nature reviews. Neuroscience · doi:10.1038/nrn1989 · Cited by 215
HDAC4 Promotes Growth of Colon Cancer Cells via Repression of p21
Wilson, A. J., Byun, D.-S., Nasser, S., Murray, L. B., Ayyanar, K., Arango, D., Figueroa, M. E., Melnick, A. M., Kao, G. D., Augenlicht, L. H., et al. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-02-0139 · Cited by 215
Rett syndrome: a neurological disorder with metabolic components
Kyle, S. M., Vashi, N., & Justice, M. J. (2018) · Open Biology · doi:10.1098/rsob.170216 · Cited by 213
HDAC7, a Thymus-Specific Class II Histone Deacetylase, Regulates Nur77 Transcription and TCR-Mediated Apoptosis
Dequiedt, F., Kasler, H. G., Fischle, W., Kiermer, V., Weinstein, M., HERNDIER, B. G., & Verdin, E. M. (2003) · Immunity · doi:10.1016/s1074-7613(03)00109-2 · Cited by 218
Self-citation
Epigenetics and Cardiovascular Development
Chang, C., & Bruneau, B. G. (2011) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020911-153242 · Cited by 203
The N-CoR/Histone Deacetylase 3 Complex Is Required for Repression by Thyroid Hormone Receptor
Ishizuka, T., & Lazar, M. A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5122-5131.2003 · Cited by 202
Self-citation
Cys2His2 zinc finger protein family: Classification, functions, and major members
Razin, S. V., Borunova, V. V., Maksimenko, O. G., & Kantidze, O. L. (2012) · Biochemistry (Moscow) · doi:10.1134/s0006297912030017 · Cited by 204
Nuclear receptor co-repressors are required for the histone-deacetylase activity of HDAC3 in vivo
You, S.-H., Lim, H., Sun, Z., Broache, M., Won, K., & Lazar, M. A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2476 · Cited by 199
Self-citation
Histone deacetylases: structural determinants of inhibitor selectivity
Micelli, C., & Rastelli, G. (2015) · Drug Discovery Today · doi:10.1016/j.drudis.2015.01.007 · Cited by 199
Signaling chromatin to make muscle
McKinsey, T. A., Zhang, C. L., & Olson, E. N. (2002) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(02)00389-7 · Cited by 198
MEF2 transcription factors: developmental regulators and emerging cancer genes
Pon, J. R., & Marra, M. A. (2015) · Oncotarget · doi:10.18632/oncotarget.6223 · Cited by 207
Histone Deacetylase 7 Associates with Hypoxia-inducible Factor 1α and Increases Transcriptional Activity
Kato, H., Tamamizu‐Kato, S., & Shibasaki, F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406320200 · Cited by 202
Class II a HDAC s – new insights into their functions in physiology and pathology
Parra, M. (2014) · FEBS Journal · doi:10.1111/febs.13061 · Cited by 197
Immunomodulatory effects of deacetylase inhibitors: therapeutic targeting of FOXP3+ regulatory T cells
Wang, L., de Zoeten, E. F., Greene, M. I., & Hancock, W. W. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd3031 · Cited by 186
Modulation of Smooth Muscle Gene Expression by Association of Histone Acetyltransferases and Deacetylases with Myocardin
Cao, D., Wang, Z., Zhang, C., Oh, J., Xing, W., Li, S., Richardson, J. A., Wang, D.-Z., & Olson, E. N. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.25.1.364-376.2005 · Cited by 185
Regulation of Androgen Receptor Activity by the Nuclear Receptor Corepressor SMRT*
Liao, G., Chen, L.-Y., Zhang, A., Godavarthy, A., Xia, F., Ghosh, J. C., Li, H., & Chen, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206374200 · Cited by 207
IκB Kinase α-Mediated Derepression of SMRT Potentiates Acetylation of RelA/p65 by p300
Hoberg, J. E., Popko, A. E., Ramsey, C. S., & Mayo, M. W. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.26.2.457-471.2006 · Cited by 183
The histone deacetylase 4/SP1/microrna-200a regulatory network contributes to aberrant histone acetylation in hepatocellular carcinoma
Yuan, J., Yang, F., Chen, B.-F., Lu, Z. J., Huo, X., Zhou, W., Wang, F., & Sun, S. (2010) · Hepatology · doi:10.1002/hep.24606 · Cited by 182
Histone deacetylase 4 interacts with 53BP1 to mediate the DNA damage response
Kao, G. D., McKenna, W. G., Guenther, M. G., Muschel, R. J., Lazar, M. A., & Yen, T. J. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200209065 · Cited by 178
Self-citation
Krüppel-like Factor-6 Promotes Preadipocyte Differentiation through Histone Deacetylase 3-dependent Repression of DLK1
Li, D., Yea, S., Li, S., Zhu, C. X., Narla, G., Banck, M. S., Laborda, J., Tan, S., Friedman, J. M., Friedman, S. L., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500463200 · Cited by 177
Hyaluronic Acid Promotes Angiogenesis by Inducing RHAMM-TGFβ Receptor Interaction via CD44-PKCδ
Park, D., Kim, Y., Kim, H., Kim, K., Lee, Y., Choe, J., Hahn, J.-H., Lee, H., Jeon, J., Choi, C., et al. (2012) · Molecules and Cells · doi:10.1007/s10059-012-2294-1 · Cited by 178
Histone Deacetylase Inhibitors In The Treatment Of Cancer: Overview And Perspectives
Giannini, G., Cabri, W., Fattorusso, C., & Rodriquez, M. (2012) · Future Medicinal Chemistry · doi:10.4155/fmc.12.80 · Cited by 182
Histone Deacetylase: A Potential Therapeutic Target for Fibrotic Disorders
Pang, M., & Zhuang, S. (2010) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.110.168385 · Cited by 173
Phosphorylation of histone deacetylase 7 by protein kinase D mediates T cell receptor–induced Nur77 expression and apoptosis
Dequiedt, F., Lint, J. V., Lecomte, E., Duppen, V. V., Seufferlein, T. T. W., Vandenheede, J. R., Wattiez, R., & Kettmann, R. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20042034 · Cited by 171
Self-citation
Histone deacetylase (HDAC) inhibitors targeting HDAC3 and HDAC1 ameliorate polyglutamine-elicited phenotypes in model systems of Huntington's disease
Jia, H., Pallos, J., Jacques, V., Lau, A., Tang, B., Cooper, A. C., Syed, A., Purcell, J. M., Chen, Y., Sharma, S., et al. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.01.016 · Cited by 173
Histone deacetylase (HDAC) 1 and 2 are essential for accurate cell division and the pluripotency of embryonic stem cells
Jamaladdin, S., Kelly, R. D., O’Regan, L., Dovey, O. M., Hodson, G. E., Millard, C. J., Portolano, N., Fry, A. M., Schwabe, J. W. R., & Cowley, S. M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321330111 · Cited by 164
Physiological Roles of Class I HDAC Complex and Histone Demethylase
Hayakawa, T., & Nakayama, J. (2010) · BioMed Research International · doi:10.1155/2011/129383 · Cited by 165
Hypoxia and angiogenesis: regulation of hypoxia-inducible factors via novel binding factors
Chen, L., Endler, A., & Shibasaki, F. (2009) · Experimental & Molecular Medicine · doi:10.3858/emm.2009.41.12.103 · Cited by 176
Chromatin Remodeling in Cardiovascular Development and Physiology
Han, P., Hang, C. T., Yang, J., & Chang, C. (2011) · Circulation Research · doi:10.1161/circresaha.110.224287 · Cited by 168
A conserved structural motif reveals the essential transcriptional repression function of Spen proteins and their role in developmental signalingPreprint
Ariyoshi, M., & Schwabe, J. W. R. (2003) · Genes & Development · doi:10.1101/gad.266203 · Cited by 163

Authors: Fischle, W., Dequiedt, F., Hendzel, M. J., Guenther, M. G., Lazar, M. A., Voelter, W., & Verdin, E.
Affiliations: University of California, San Francisco (US)
University of Alberta (CA)
University of Pennsylvania (US)
University of Tübingen (DE)
Corresponding author: Verdin, Eric
ORCID: Fischle, Wolfgang
Hendzel, Michael J
Guenther, Matthew G
Lazar, Mitchell A
Voelter, Wolfgang
Verdin, Eric
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2002-01
Volume: 9
Issue: 1
Pages: 45-57
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/s1097-2765(01)00429-4
OpenAlex: W2052373759
Cited by: 754
References: 60
Citations by year: 2026: 16 · 2025: 20 · 2024: 26 · 2023: 12 · 2022: 32 · 2021: 23 · 2020: 31 · 2019: 39 · 2018: 29 · 2017: 34 · 2016: 33 · 2015: 43 · 2014: 42 · 2013: 46 · 2012: 41
FWCI: 9.99
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 4215 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Molecular Cell (publishedVersion)
PubMed (publishedVersion)
MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
Max Planck Institute for Plasma Physics (submittedVersion)
Open Repository and Bibliography (University of Liège) (submittedVersion)
Funders: National Institute of General Medical Sciences (R01GM051671, GM51671)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
Keywords: histone deacetylase, class II HDACs, HDAC4, HDAC3, SMRT, NCoR, corepressors, protein complexes, transcriptional repression, gene expression regulation, repressors
MeSH terms: Histone Deacetylase 3, Amino Acid Sequence, DNA Mutational Analysis, DNA-Binding Proteins, Enzyme Activation, HeLa Cells, Histone Deacetylases, Humans, Molecular Sequence Data, Protein Binding, Repressor Proteins, Transcription, Genetic, Nuclear Receptor Co-Repressor 2

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Enzymatic Activity Associated with Class II HDACs Is Dependent on a Multiprotein Complex Containing HDAC3 and SMRT/N-CoR

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks